Information on EC 3.4.23.B10 - Rous sarcoma virus retropepsin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.23.B10
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
Rous sarcoma virus retropepsin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
The cleavage sequence in the natural substrate NC-PR is PPAVS-/-LAMTMRR. The activity can be improved by substitution by Trp, Tyr, Phe, Leu, Arg, Glu, His or Ala in P1, Tyr in P3', and Arg, Phe, Asn or His in P3
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
144114-21-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
strain Prague C
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Gag polyprotein precursor + H2O
?
show the reaction diagram
gag precursor polyprotein + H2O
?
show the reaction diagram
Gag-Pol precursor polyprotein + H2O
?
show the reaction diagram
GAVSLAMT + H2O
GAVS + LAMT
show the reaction diagram
-
-
-
?
KARVLAEAMS + H2O
KARVL + AEAMS
show the reaction diagram
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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?
PARVLAEAMRR + H2O
PARVL + AEAMRR
show the reaction diagram
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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?
PARVLFLDGRR + H2O
PARVL + FLDGRR
show the reaction diagram
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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?
PASSLAMT + H2O
PASS + LAMT
show the reaction diagram
-
-
-
?
PATIMMORERR + H2O
PATIM + MORERR
show the reaction diagram
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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?
PATVLTVALRR + H2O
PATVL + TVALRR
show the reaction diagram
PAVSLAMT + H2O
PAVS + LAMT
show the reaction diagram
PAVYLAMT + H2O
PAVY + LAMT
show the reaction diagram
-
-
-
?
PFQAYPLREA + H2O
PFQAY + PLREA
show the reaction diagram
-
-
-
-
?
PFVSLAMT + H2O
PFVS + LAMT
show the reaction diagram
-
-
-
?
PGNFLQSRR + H2O
PGNF + LQSRR
show the reaction diagram
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
-
?
PHAVSLAMTMRR + H2O
PHAVS + LAMTMRR
show the reaction diagram
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-
-
-
?
PPAVALAMTMRR + H2O
PPAVA + LAMTMRR
show the reaction diagram
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
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-
?
PPAVELAMTMRR + H2O
PPAVE + LAMTMRR
show the reaction diagram
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
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-
?
PPAVFLAMTMRR + H2O
PPAVF + LAMTMRR
show the reaction diagram
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
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-
?
PPAVHLAMTMRR + H2O
PPAVH + LAMTMRR
show the reaction diagram
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
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-
?
PPAVLLAMTMRR + H2O
PPAVL + LAMTMRR
show the reaction diagram
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
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-
?
PPAVRLAMTMRR + H2O
PPAVR + LAMTMRR
show the reaction diagram
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPAVSLAMTMRR + H2O
PPAVS + LAMTMRR
show the reaction diagram
PPAVSLAYMRR + H2O
PPAVS + LAYTMRR
show the reaction diagram
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
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-
?
PPAVWLAMTMRR + H2O
PPAVW + LAMTMRR
show the reaction diagram
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
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-
?
PPAVYLAMTMRR + H2O
PPAVY + LAMTMRR
show the reaction diagram
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
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-
?
PPDVSLAMTMRR + H2O
PPDVS + LAMTMRR
show the reaction diagram
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slight increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
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-
?
PPFVSLAMTMRR + H2O
PPFVS + LAMTMRR
show the reaction diagram
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPHVSLAMTMRR + H2O
PPHVS + LAMTMRR
show the reaction diagram
PPNVSLAMTMRR + H2O
PPNVS + LAMTMRR
show the reaction diagram
PPRVSLAMTMRR + H2O
PPRVS + LAMTMRR
show the reaction diagram
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
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-
?
Rous sarcoma virus glycoprotein precursor + H2O
?
show the reaction diagram
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the enzyme has a stringent requirement for the presence of a pair of basic residues (Arg-Arg or Lys-Arg), when the cleavage sequence is deleted or modified to contain unpaired basic residues, intracellular cleavage of the glycoprotein precursor is completely blocked
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-
?
TFQAYPLREA + H2O
TFQAY + PLREA
show the reaction diagram
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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?
TLNFPISPKK + H2O
TLNF + PISPKK
show the reaction diagram
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slow cleavage with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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?
TSCYHCGT + H2O
TSCY + HCGT
show the reaction diagram
-
-
-
?
VFQNYPIVQ + H2O
VFQNY + PIVQ
show the reaction diagram
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medium-sized or large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
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-
?
VIQNYPIVQ + H2O
VIQNY + PIVQ
show the reaction diagram
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medium-sized or large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
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-
?
VLQNYPIVQ + H2O
VLQNY + PIVQ
show the reaction diagram
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medium-sized or large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
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-
?
VSFNFPQITKK + H2O
VSFNF + PQITKK
show the reaction diagram
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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?
VSFNYPIVQ + H2O
VSFNY + PIVQ
show the reaction diagram
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Phe and Leu are preferred at position P3
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-
?
VSLNYPIVQ + H2O
VSLNY + PIVQ
show the reaction diagram
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Phe and Leu are preferred at position P3
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-
?
VSQNAPIVQ + H2O
VSQNA + PIVQ
show the reaction diagram
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preference order for P1 position is Phe > Tyr > Leu, Met > Ala
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-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
show the reaction diagram
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preference order for P1 position is Phe > Tyr > Leu, Met > Ala
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-
?
VSQNLPIVQ + H2O
VSQNL + PIVQ
show the reaction diagram
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preference order for P1 position is Phe > Tyr > Leu, Met > Ala
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-
?
VSQNMPIVQ + H2O
VSQNM + PIVQ
show the reaction diagram
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preference order for P1 position is Phe > Tyr > Leu, Met > Ala
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?
VSQNYPIVQ + H2O
VSQNY + PIVQ
show the reaction diagram
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preference order for P1 position is Phe > Tyr > Leu, Met > Ala
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Gag polyprotein precursor + H2O
?
show the reaction diagram
gag precursor polyprotein + H2O
?
show the reaction diagram
Gag-Pol precursor polyprotein + H2O
?
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Arg-Val-Leu-r-Phe-Glu-Ala-Nle-NH2
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mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
additional information
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Arg-Val-Leu-(reduced bond)-Phe-Glu-Ale-Nle-NH2 inhibits mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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the p2 region of RSV Gag, particularly the Pro-Pro-Pro-Tyr motif is important in the processing of the gag precursor polyprotein, most probably by controlling the activation of the virally encoded protease
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011 - 0.064
GAVSLAMT
0.244
KARVLAEAMS
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.366
PARVLAEAMRR
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pH 5.9, 37C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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0.111
PARVLFLDGRR
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pH 5.9, 37C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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0.006 - 2.4
PASSLAMT
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0.132
PATIMMORERR
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pH 5.9, 37C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.009 - 0.056
PAVSLAMT
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24.5
PAVYLAMT
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pH 5.9, 37C, wild-type enzyme
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0.004 - 0.0054
PFVSLAMT
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0.283
PGNFLQSRR
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pH 5.9, 37C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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0.006 - 0.077
PPAVSLAMTMRR
0.095 - 0.1
PRKILFLDGRR
0.037
TFQAYPLREA
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.072 - 427
TSCYHCGT
0.538
VSFNFPQITKK
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0483 - 0.36
GAVSLAMT
0.167
KARVLAEAMS
Rous sarcoma virus
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
1.63
PARVLAEAMRR
Rous sarcoma virus
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pH 5.9, 37C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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8.2
PARVLFLDGRR
Rous sarcoma virus
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pH 5.9, 37C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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0.0717 - 0.217
PASSLAMT
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2.98
PATIMMORERR
Rous sarcoma virus
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pH 5.9, 37C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.273 - 0.613
PAVSLAMT
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4.07
PAVYLAMT
Rous sarcoma virus
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pH 5.9, 37C
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0.248 - 0.437
PFVSLAMT
-
0.283
PGNFLQSRR
Rous sarcoma virus
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pH 5.9, 37C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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0.0183 - 1.6
PPAVSLAMTMRR
0.0217 - 0.193
PRKILFLDGRR
0.183
TFQAYPLREA
Rous sarcoma virus
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.147 - 1.23
TSCYHCGT
0.25
VSFNFPQITKK
Rous sarcoma virus
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
additional information
additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000487
Arg-Val-Leu-r-Phe-Glu-Ala-Nle-NH2
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mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
additional information
additional information
-
Ki-value for Arg-Val-Leu-(reduced bond)-Phe-Glu-Ale-Nle-NH2 is 0.00002 mM, mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
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A40S mutant enzyme, reaction with PPAVSLAMTMRR
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
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pH 5: about 60% of maximal activity, pH 8: about 10% of maximal activity, A40S mutant enzyme, reaction with PPAVSLAMTMRR
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme sequence, or p10 sequence, contains a leptomycin B-dependent nuclear-export-signal, NES
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the enzyme sequence, or p10 sequence of the Gag polyprotein, contains a leptomycin B-dependent nuclear-export-signal, NES, involving residues L219, W222, V225, and L229, the NES sequence is positionally independent and transferable, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
free or ligated enzyme, structure analysis in comparison to HIV-1 retropepsin
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free or ligated wild-type and mutant enzymes, structure analysis in comparison to HIV-1 retropepsin
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mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N crystallized with an inhibitor of HIV-1 protease, Arg-Val-Leu-(reduced bond)-Phe-Glu-Ala-Nle-NH2. A polyhistidine sequence is added to the amino terminus of the enzyme to allow for efficient and rapid purification
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the multiple substitution allow the protease to cleave four HIV-1 peptide substrates at initial rates more than 100fold greater than wild-type enzyme
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant and wild-type enzymes
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native enzyme from whole virus
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recombinant wild-type and mutant enzymes from Escherichia coli with refolding from inclusion bodies to over 95% purity, N-terminally His-tagged enzyme from Escherichia coli soluble fraction by nickel affinity chromatography
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wild-type and mutant linked-dimer RSV protease
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in silkworm larvae
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expression of wild-type and mutant enzymes in DF-1 cells
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expression of wild-type and mutant enzymes in Escherichia coli in inclusion bodies, expression of N-terminally His-tagged enzyme in Escherichia coli in the soluble fraction
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expression of wild-type and mutant Gag polyprotein fused to GFP in QT6 cells
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wild-type and histidine-tagged mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N are expressed in Escherichia coli M15 pDM1
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S38T/I42D/I44V/M73V/A100L/V104T/R105P/G106V/S107N
A40S
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mutant enzyme shows 23% of the activity compared to wild-type enzyme with PPAVSLAMTMRR
A40T
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mutant enzyme is inactive with PPAVSLAMTMRR
D37S
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mutant enzyme is inactive with PPAVSLAMTMRR
DELTAN61-Q63
H65G
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mutant enzyme is inactive with PPAVSLAMTMRR
H65G/R105P/G106V
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mutant enzyme shows about 25% of the activity of the wild-type enzyme in RSV substrates, about 5fold higher activity with the HIV-1 peptide substrate PRKILFLDGRR
L180A/L184A/V187A
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site-directed mutagenesis of the Gag polyprotein p10 sequence residues, the mutant protein shows normal nucleocytoplasmic trafficking and localization at the cell plasmamembrane and in the cytosol
L219A
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site-directed mutagenesis of the Gag polyprotein p10 sequence residue leads to accumulation of the mutant protein in the nucleus and reduced virus assembly, overview
L229A
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site-directed mutagenesis of the Gag polyprotein p10 sequence residue leads to accumulation of the mutant protein in the nucleus and reduced virus assembly, overview
M239F
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site-directed mutagenesis of the p10-capsid protease sequence of Gag polyprotein does not affect the enzyme activity and virus replication
M239G
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site-directed mutagenesis of the p10-capsid protease sequence of Gag polyprotein abolishes the enzyme activity and blocks Rous sarcoma virus replication, detrimental effect, overview
M73V/A100L
N61P/P62L/Q63M
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mutant enzyme shows 434% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
P240F
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site-directed mutagenesis of the p10-capsid protease sequence of Gag polyprotein abolishes the enzyme activity and blocks Rous sarcoma virus replication, detrimental effect, overview
R105P/G106V
R105P/G106V/H65G
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mutant enzyme exhibits behavior very similar to the wild-type enzyme for substitutions in the P4, P3, P2, P2', and P3' of the PPAVSLAMTMRR substrate positions. In contrast the mutants behave more like the HIV-1 protease in preference for amino acids substituted in the P1 and P1' positions
R105P/G106V/S107N
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cleaves TSCYHCGT 50fold faster than the wild-type enzyme, cleaves PASSLAMT 140fold faster than the wild-type enzyme, cleaves PAVSLAMT 13.7fold faster than the wild-type enzyme, cleaves GAVSLAMT 48fold faster than the wild-type enzyme, cleaves PFVSLAMT 2.6fold faster than the wild-type enzyme; mutant enzyme shows 738% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
S38T
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200% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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the murtant enzyme has 9 structurally equivalent residues from HIV-1 protease. Unlike the wild-type enzyme, the mutant enzyme hydrolyzes peptides representing the HIV-1 protease polyprotein cleavage sites
S38T/I42D/I44V/M73V/A100L/V104T/R105P/G106V/S107N
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site-directed mutagenesis leading to the mutant RSV S9 protease, which is active with HIV-1 retropepsin substrates and inhibitable by HIV-1 retropepsin-specific inhibitors in contrast to the wild-type enzyme
V104T/R105P/G106V/S107N
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mutant enzyme shows 496% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
V225A
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site-directed mutagenesis of the Gag polyprotein p10 sequence residue leads to accumulation of the mutant protein in the nucleus and reduced virus assembly, overview
V241G
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site-directed mutagenesis of the p10-capsid protease sequence of Gag polyprotein abolishes the enzyme activity and blocks Rous sarcoma virus replication, detrimental effect, overview
W222A
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site-directed mutagenesis of the Gag polyprotein p10 sequence residue leads to accumulation of the mutant protein in the nucleus and reduced virus assembly, overview
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzymes expressed in Escherichia coli, refolding from inclusion bodies
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis